Tiziana Bonaldi is Tenured Group Leader at the Department of Experimental Oncology of the IEO (Milan, Italy), where she directs the Giovanni Armenise-Harvard Foundation Laboratory on “Nuclear proteomics to gene expression regulation”.
Following a PhD in Molecular and Cellular Biology in Milan, she joined A. Imhof at the LMU in Munich, where –as post doc- she pioneered the use MS for the characterisation of histone code.
With a second post-doctoral research in M. Mann’s group of at the MPI of Biochemistry, she focused on post-transcriptional regulation of gene expression.
When starting her independent research at IEO in 2008, she strengthened her expertise in applying proteomics to study multi-layered gene expression regulation, establishing innovative studies for the analysis of chromatin composition and histone modifications from primary patient specimens; the systematic investigation of the methyl-proteome and of microRNA effect in cancer. She has published 54 peer-review scientific papers, with an h-index of 25 (WoS).
She received the “Armenise-Harvard Career Development Award” in 2007 and the “International Inner Wheel for Women, for scientific achievements” in 2010. In 2014 she successfully completed her tenure-track and was appointed as Associate Professor at IEO.

The role of non-histone protein arginine (R) methylation has been established in almost every aspect of cellular biology and its deregulation correlates with diverse pathological conditions, including cancer (1). Building on our recent evidence of the recurrence of this post translational modification (PTM) both on proteins involved in the DNA damage response (DDR) and on several subunits of the Large Drosha Complex (LDC) (2), we developed two studies aiming at the molecular and functional characterization of R-methylation in these biological processes.
I will present recent unpublished data on the systematic identification of PRMT1 substrates, through an analytical strategy combining heavy-methyl and standard SILAC, followed by ad hoc data analysis pipeline. Through quantitative profiling of the methyl-proteome dynamics during the DNA damage response (DDR) we showed that PRMT1 accumulation on chromatin during DDR correlates with global R-methylations changes of both histone and non-histone proteins and that PRMT1-dependent methylation changes massively affect the LDC structure and function, causing the overall impairment of microRNA synthesis.